scholarly journals Antisense Oligonucleotides Targeting Parasite Inositol 1,4,5-Trisphosphate Receptor Inhibits Mammalian Host Cell Invasion by Trypanosoma cruzi

2014 ◽  
Vol 4 (1) ◽  
Author(s):  
Muneaki Hashimoto ◽  
Takeshi Nara ◽  
Hiroko Hirawake ◽  
Jorge Morales ◽  
Masahiro Enomoto ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Antisense Oligonucleotides ◽  
Mammalian Host ◽  
Host Cell Invasion ◽  
Inositol 1,4,5 Trisphosphate ◽  
Trisphosphate Receptor

scholarly journals Molecular Characterization of a Novel Family of Trypanosoma cruzi Surface Membrane Proteins (TcSMP) Involved in Mammalian Host Cell Invasion

2015 ◽  
Vol 9 (11) ◽  
pp. e0004216 ◽  
Author(s):  
Nadini Oliveira Martins ◽  
Renata Torres de Souza ◽  
Esteban Mauricio Cordero ◽  
Danielle Cortez Maldonado ◽  
Cristian Cortez ◽  
...  
Keyword(s):  
Membrane Proteins ◽  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Molecular Characterization ◽  
Cell Invasion ◽  
Surface Membrane ◽  
Mammalian Host ◽  
Host Cell Invasion

scholarly journals Fibronectin-Degrading Activity of Trypanosoma cruzi Cysteine Proteinase Plays a Role in Host Cell Invasion

2014 ◽  
Vol 82 (12) ◽  
pp. 5166-5174 ◽  
Author(s):  
Fernando Yukio Maeda ◽  
Cristian Cortez ◽  
Mario Augusto Izidoro ◽  
Luiz Juliano ◽  
Nobuko Yoshida
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Hela Cells ◽  
Transforming Growth Factor ◽  
Cysteine Proteinase ◽  
Mammalian Host ◽  
Cysteine Proteinase Inhibitor ◽  
Host Cell Invasion ◽  
Content Type

ABSTRACTTrypanosoma cruzi, the agent of Chagas disease, binds to diverse extracellular matrix proteins. Such an ability prevails in the parasite forms that circulate in the bloodstream and contributes to host cell invasion. Whether this also applies to the insect-stage metacyclic trypomastigotes, the developmental forms that initiate infection in the mammalian host, is not clear. UsingT. cruziCL strain metacyclic forms, we investigated whether fibronectin bound to the parasites and affected target cell invasion. Fibronectin present in cell culture medium bound to metacyclic forms and was digested by cruzipain, the majorT. cruzicysteine proteinase. G strain, with negligible cruzipain activity, displayed a minimal fibronectin-degrading effect. Binding to fibronectin was mediated by gp82, the metacyclic stage-specific surface molecule implicated in parasite internalization. When exogenous fibronectin was present at concentrations higher than cruzipain can properly digest, or fibronectin expression was stimulated by treatment of epithelial HeLa cells with transforming growth factor beta, the parasite invasion was reduced. Treatment of HeLa cells with purified recombinant cruzipain increased parasite internalization, whereas the treatment of parasites with cysteine proteinase inhibitor had the opposite effect. Metacyclic trypomastigote entry into HeLa cells was not affected by anti-β1 integrin antibody but was inhibited by anti-fibronectin antibody. Overall, our results have indicated that the cysteine proteinase ofT. cruzimetacyclic forms, through its fibronectin-degrading activity, is implicated in host cell invasion.

scholarly journals Deletion of a Golgi protein in Trypanosoma cruzi reveals a critical role for Mn2+ in protein glycosylation needed for host cell invasion and intracellular replication

2021 ◽  
Vol 17 (3) ◽  
pp. e1009399
Author(s):  
Srinivasan Ramakrishnan ◽  
Linn M. Unger ◽  
Rodrigo P. Baptista ◽  
Teresa Cruz-Bustos ◽  
Roberto Docampo
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Critical Role ◽  
Protein Glycosylation ◽  
Growth Defect ◽  
Mammalian Host ◽  
Host Cell Invasion ◽  
Intracellular Replication ◽  
Parasite Life Cycle

Trypanosoma cruzi is a protist parasite and the causative agent of American trypanosomiasis or Chagas disease. The parasite life cycle in its mammalian host includes an intracellular stage, and glycosylated proteins play a key role in host-parasite interaction facilitating adhesion, invasion and immune evasion. Here, we report that a Golgi-localized Mn2+-Ca2+/H+ exchanger of T. cruzi (TcGDT1) is required for efficient protein glycosylation, host cell invasion, and intracellular replication. The Golgi localization was determined by immunofluorescence and electron microscopy assays. TcGDT1 was able to complement the growth defect of Saccharomyces cerevisiae null mutants of its ortholog ScGDT1 but ablation of TcGDT1 by CRISPR/Cas9 did not affect the growth of the insect stage of the parasite. The defect in protein glycosylation was rescued by Mn2+ supplementation to the growth medium, underscoring the importance of this transition metal for Golgi glycosylation of proteins.

scholarly journals Host cell invasion and oral infection by Trypanosoma cruzi strains of genetic groups TcI and TcIV from chagasic patients

2016 ◽  
Vol 9 (1) ◽  
Author(s):  
Fernando Yukio Maeda ◽  
Tatiana Mordente Clemente ◽  
Silene Macedo ◽  
Cristian Cortez ◽  
Nobuko Yoshida
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Oral Infection ◽  
Host Cell Invasion ◽  
Genetic Groups

scholarly journals Expression and Cellular Localization of Molecules of the gp82 Family in Trypanosoma cruzi Metacyclic Trypomastigotes

2007 ◽  
Vol 75 (7) ◽  
pp. 3264-3270 ◽  
Author(s):  
Vanessa D. Atayde ◽  
Mauro Cortez ◽  
Renata Souza ◽  
José Franco da Silveira ◽  
Nobuko Yoshida
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Cellular Localization ◽  
Polyclonal Antibodies ◽  
Microscopic Analysis ◽  
Cdna Clones ◽  
Host Cell Invasion ◽  
Two Dimensional Gel Electrophoresis ◽  
Surface Localization

ABSTRACT A member of the Trypanosoma cruzi gp82 family, expressed on metacyclic trypomastigote surface and identified by monoclonal antibody (MAb) 3F6, plays a key role in host cell invasion. Apart from the gp82 defined by MAb 3F6, no information is available on members of this protein family. From cDNA clones encoding gp82 proteins sharing 59.1% sequence identity, we produced the recombinant proteins J18 and C03, the former containing and the latter lacking the epitope for MAb 3F6. Polyclonal antibodies to J18 and C03 proteins were generated and used, along with MAb 3F6, to analyze the expression and cellular localization of gp82 family members in metacyclic forms of CL and G strains, which belong to highly divergent genetic groups. By two-dimensional gel electrophoresis and immunoblotting, molecules of 82 to 86 kDa, focusing at pH 4.6 to 5.4, and molecules of 72 to 88 kDa, focusing at pH 4.9 to 5.7, were visualized in CL and G strains, respectively. Flow cytometry and microscopic analysis revealed in both strains similar expression of MAb 3F6-reactive gp82 in live and permeabilized parasites, indicating its surface localization. The reaction of live parasites of both strains with anti-J18 antibodies was weaker than with MAb 3F6 and was increased by permeabilization. Anti-C03 antibodies bound predominantly to flagellar components in permeabilized G strain parasites, but in the CL strain the flagellum was not the preferential target for these antibodies. Host cell invasion of metacyclic forms was inhibited by J18 protein, as well as by MAb 3F6 and anti-J18 antibodies, but not by C03 protein or anti-C03 antibodies.

scholarly journals Features of host cell invasion by different infective forms of Trypanosoma cruzi

1999 ◽  
Vol 94 (suppl 1) ◽  
pp. 135-137 ◽  
Author(s):  
Renato A Mortara ◽  
Daniela O Procópio ◽  
Helena C Barros ◽  
Newton V Verbisck ◽  
Walter K Andreoli ◽  
...  
Keyword(s):  
Trypanosoma Cruzi ◽  
Host Cell ◽  
Cell Invasion ◽  
Host Cell Invasion
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